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Blood, 27 August 2009, Vol. 114, No. 9, pp. 1904-1912. Prepublished online as a Blood First Edition Paper on June 30, 2009; DOI 10.1182/blood-2009-02-203216. This Article Full Text (PDF) Supplemental Table and Figures All Versions of this Article: blood-2009-02-203216v1 114/9/1904    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Google Scholar Articles by Anong, W. A. Articles by Low, P. S. PubMed PubMed Citation Articles by Anong, W. A. Articles by Low, P. S. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted February 2, 2009 Accepted June 18, 2009 Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion William A. Anong, Taina Franco, Haiyan Chu, Tahlia L. Weis, Emily E. Devlin, David M. Bodine, Xiuli An, Narla Mohandas, and Philip S. Low* Department of Chemistry, Purdue University, West Lafayette, IN, United States Genetics and Molecular Biology Branch, NHGRI, NIH, Bethesda, MD, United States Laboratory of Physiology, New York Blood Center, New York, NY, United States * Corresponding author; email: plow{at}purdue.edu. The erythrocyte membrane skeleton is the best understood cytoskeleton. Because its protein components have homologs in virtually all other cells, the membrane serves as a fundamental model of biological membranes. Modern textbooks portray the membrane as a two-dimensional spectrin-based membrane skeleton attached to a lipid bilayer through two linkages: band 3-ankyrin--spectrin and glycophorin C-protein 4.1--spectrin1-7. Although evidence supports an essential role for the first bridge in regulating membrane cohesion, rupture of the glycophorin C-protein 4.1 interaction has little effect on membrane stability 8. We demonstrate the existence of a novel band 3-adducin-spectrin bridge that connects the spectrin/actin/protein 4.1 junctional complex to the bilayer. As rupture of this bridge leads to spontaneous membrane fragmentation, we conclude that the band 3-adducin-spectrin bridge is important to membrane stability. The required relocation of part of the band 3 population to the spectrin/actin junctional complex and its formation of a new bridge with adducin necessitates a significant revision of accepted models of the erythrocyte membrane. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. F. Hoffman, A. Dodson, and F. Proverbio On the functional use of the membrane compartmentalized pool of ATP by the Na+ and Ca++ pumps in human red blood cell ghosts J. Gen. Physiol., September 28, 2009; 134(4): 351 - 361. [Abstract] [Full Text] [PDF]

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